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Abstract
The antifungal activity of 5‐hydroxy‐4‐oxo‐L‐norvaline (HONV), exhibited under conditions mimicking human serum, may be improved upon incorporation of this amino acid into a dipeptide structure. Several HONV‐containing dipeptides inhibited growth of human pathogenic yeasts of the Candida genus in the RPMI‐1640 medium, with minimal inhibitory concentration values in the 32 to 64 μg mL−1 range. This activity was not affected by multidrug resistance that is caused by overexpression of genes encoding drug efflux proteins. The mechanism of antifungal action of HONV dipeptides involved uptake by the oligopeptide transport system, subsequent intracellular cleavage by cytosolic peptidases, and inhibition of homoserine dehydrogenase by the released HONV. The relative transport rates determined the anticandidal activity of HONV dipeptides.
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- Category:
- Articles
- Type:
- artykuł w czasopiśmie wyróżnionym w JCR
- Published in:
-
JOURNAL OF PEPTIDE SCIENCE
no. 24,
edition 1,
pages 1 - 10,
ISSN: 1075-2617 - Language:
- English
- Publication year:
- 2018
- Bibliographic description:
- Skwarecki A., Schielmann M., Martynow D., Kawczyński M., Wiśniewska A., Milewska M., Milewski S.: Antifungal dipeptides incorporating an inhibitor of homoserine dehydrogenase// JOURNAL OF PEPTIDE SCIENCE. -Vol. 24, iss. 1 (2018), s.1-10
- DOI:
- Digital Object Identifier (open in new tab) 10.1002/psc.3060
- Verified by:
- Gdańsk University of Technology
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